By Hugo O. Villar (Eds.)
The second one quantity in a chain which goals to target advances in computational biology. This quantity discusses such issues as: statistical research of protein sequences; growth in large-scale series research; and the structure of loops in proteins
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Extra resources for Advances in Computational Biology
In some cases the original molecular structure of the molecule is sufficient to give a complete channel and no self-assembly in the bilayer is therefore required. Another possibility is the self-assembly of channel-forming protein 'monomers' (already dissolved in the bilayer) via lateral diffusion and nonspecific protein-protein association. The latter includes steric interactions between the channel-forming monomers themselves and between channel-forming monomers and the surrounding lipid matrix.
The range over which the fluctuations are operative is described by a coherence length which is a measure of the average domain size. The average domain size depends on temperature and attains a maximum at the gel-to-fluid phase transition. For example for DPPC bilayers, the actual lipid-domain size may become as large as several hundred lipid molecules. Hence, the dynamic membrane heterogeneity leads to membrane organization on a mesoscopic length scale. The Computation of Lipid-Protein Interactions 39 w*^^\ (a) (b) Figure 8.
Above this critical value, the main transition is of first order and below this value there is no phase transition. F(A, T, L), derived from the distribution function for the membrane area, A, was calculated for several values of the mismatch parameter to examine the phase behavior of the system and to locate the critical point. It was found that the model did not exhibit a phase transition for values of F^ below 4 x KT^^erg/A. At this value of F^, the system is at, or extremely close to, the critical point.
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